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- W2912941483 abstract "Myosin, the molecular motor of muscle, is composed of two identical heavy chains and two different light chains, the essential light chain (Mlc1) and the regulatory light chain. The light chains are part of the myosin lever arm, which is critical for generating force and motion. Drosophila has a single Mlc1 gene that is alternatively spliced into two isoforms. To investigate the function of these Mlc1 isoforms in muscle mechanical properties, such as stretch activation and in enabling the fastest known frequency of muscle contraction, we created a Drosophila null for Mlc1 using the CRISPR/Cas9 system. To our surprise, we found that Mlc1 homozygous null embryos hatched, crawled and molted. Sequencing confirmed that we had targeted Mlc1. The resulting Mlc1 null line contains a two-nucleotide deletion, which truncates Mlc1 after 85 amino acids. Mlc1 mutant larvae crawling velocity was reduced by ∼50% compared to wild-type. Approximately 50% of Mlc110 larvae pupariate, of these at least 50% progress through metamorphosis, but only 8% eclose and survive to adulthood. Fiber level IFM and TDT muscle structure appeared normal in Mlc1 null adults, but they were unable to fly or jump. Skinned IFM fibers isolated from 1 or 3 day old null flies did not activate or produce power. Transformation with a 4.099 kb DNA fragment containing the genomic locus of Mlc1 with 5’ and 3’ UTR rescued adult viability, crawling velocity, and IFM power production to wild-type levels. We are currently performing experiments to determine if another protein is replacing Mlc1 on the myosin lever arm in the null line. We conclude that Mlc1 is not essential for embryonic and larval muscle development and function." @default.
- W2912941483 created "2019-02-21" @default.
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- W2912941483 date "2019-02-01" @default.
- W2912941483 modified "2023-09-30" @default.
- W2912941483 title "The Muscle Myosin Essential Light Chain is Not Essential for Muscle Function" @default.
- W2912941483 doi "https://doi.org/10.1016/j.bpj.2018.11.983" @default.
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